2ZSH

Structural basis of gibberellin(GA3)-induced DELLA recognition by the gibberellin receptor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0009739	biological_process	response to gibberellin
A	0009939	biological_process	positive regulation of gibberellic acid mediated signaling pathway
A	0010325	biological_process	raffinose family oligosaccharide biosynthetic process
A	0010331	molecular_function	gibberellin binding
A	0010476	biological_process	gibberellin mediated signaling pathway
A	0016787	molecular_function	hydrolase activity
A	0048444	biological_process	floral organ morphogenesis
A	0048530	biological_process	fruit morphogenesis
A	0071456	biological_process	cellular response to hypoxia
A	1905516	biological_process	positive regulation of fertilization

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE GA3 A 345

Chain	Residue
A	PHE27
A	ASP243
A	ARG244
A	TYR247
A	VAL319
A	GLY320
A	TYR322
A	HOH364
A	HOH458
A	ARG35
A	GLY115
A	SER116
A	TYR127
A	ASP190
A	SER191
A	PHE238
A	VAL239

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Functional Information from PROSITE/UniProt

site_id	PS01173
Number of Residues	17
Details	LIPASE_GDXG_HIS Lipolytic enzymes "G-D-X-G" family, putative histidine active site. ILfFHGGSFahsSanSA

Chain	Residue	Details
A	ILE109-ALA125

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site_id	PS01174
Number of Residues	13
Details	LIPASE_GDXG_SER Lipolytic enzymes "G-D-X-G" family, putative serine active site. IfLAGDSSGGnIA

Chain	Residue	Details
A	ILE185-ALA197

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:Q0ZPV7, ECO:0000255|PROSITE-ProRule:PRU10038

Chain	Residue	Details
A	SER191
A	ASP289

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site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:19037309, ECO:0007744|PDB:2ZSI

Chain	Residue	Details
A	GLY115
A	TYR127
A	SER191
A	GLY320

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:19037309, ECO:0007744|PDB:2ZSH

Chain	Residue	Details
A	SER116
A	PHE238

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:Q9LT10

Chain	Residue	Details
A	ALA2

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